Figure 2: Structure of Cphy1178_20–462.

(A) Secondary structure cartoon of a monomer of Cphy1178_20–462 showing bound NAD⁺ as spheres coloured yellow for carbon, red for oxygen, blue for nitrogen and orange for phosphorus. The catalytic domain is highlighted in pink, rossman fold nucleotide binding domain in grey and oligomerisation domain in green. (B) Active site tunnel and nucleotide binding pocket. The surface of Cphy1178_20–462 is shown coloured by electrostatic potential (blue for positive, red for negative) and the secondary structure cartoon is shown in blue. The catalytic cysteine and histidine residues are shown as sticks. Bound cofactors, NAD⁺ and CoA are shown with yellow and pink carbons respectively. (C) Cphy1178 forms a dimer of dimers quaternary structure. Two subunits are shown as cartoons, with NAD⁺ shown as spheres to show the relative orientation of the nucleotide-binding cleft; two further subunits are shown as grey surface representations.